Results 31 to 40 of about 3,112 (224)

PIGO‐CDG: A case study with a new genotype, expansion of the phenotype, literature review, and nosological considerations

JIMD Reports, 2023
The phosphatidylinositol glycan anchor biosynthesis class O protein (PIGO) enzyme is an important step in the biosynthesis of glycosylphosphatidylinositol (GPI), which is essential for the membrane anchoring of several proteins.
Rodrigo Tzovenos Starosta, Nino Kerashvili, Cassandra Pruitt, Matthew J. Schultz, Suzanne W. Boyer, Eva Morava, Maria Laura Duque Lasio, Dorothy K. Grange   +7 more
doaj   +1 more source

Novel insights into the phenotype and long-term D-gal treatment in PGM1-CDG: a case series

Therapeutic Advances in Rare Disease, 2023
Phosphoglucomutase-1-congenital disorder of glycosylation (PGM1-CDG) (OMIM: 614921) is a rare autosomal recessive inherited metabolic disease caused by the deficiency of the PGM1 enzyme. Like other CDGs, PGM1-CDG has a multisystemic presentation.
Silvia Radenkovic, Christin Johnsen, Andreas Schulze, Gurnoor Lail, Laura Guilder, Kaitlin Schwartz, Matthew Schultz, Saadet Mercimek-Andrews, Suzanne Boyer, Eva Morava   +9 more
doaj   +1 more source

GMPPB-CDG Results in Lysosomal Dysfunction and Acid Alpha-Glucosidase Deficiency. [PDF]

J Inherit Metab Dis
ABSTRACT GDP‐mannose pyrophosphorylase B (GMPPB) deficiency is a congenital disorder of glycosylation due to pathogenic variants of the GMPPB gene. GMPPB catalyzes GDP‐mannose synthesis, an early step in multiple glycosylation pathways, including N‐glycosylation, O‐mannosylation, C‐mannosylation, and glycosylphosphatidylinositol‐anchor formation.
Damiano C, Tarallo A, Gragnaniello V, Strollo S, Fecarotta S, Tuzzi MR, Polishchuk E, Montefusco S, Valanzano A, Assunto A, Minopoli N, Casa RD, Polishchuk R, Groen SLMI', Medina DL, Bertini E, Carrozzo R, Emmerich J, Schoser B, Pijnappel WWMP, Parenti G.   +20 more
europepmc   +2 more sources

Insufficient ER-stress response causes selective mouse cerebellar granule cell degeneration resembling that seen in congenital disorders of glycosylation [PDF]

, 2013
BACKGROUND: Congenital disorders of glycosylation (CDGs) are inherited diseases caused by glycosylation defects. Incorrectly glycosylated proteins induce protein misfolding and endoplasmic reticulum (ER) stress.
Huaxi Xu, Hudson H Freeze, Kun Zhou, Liangwu Sun, Yingjun Zhao, Yun-wu Zhang   +5 more
core   +1 more source

Global serum glycoform profiling for the investigation of dystroglycanopathies & Congenital Disorders of Glycosylation [PDF]

, 2016
The Congenital Disorders of Glycosylation (CDG) are an expanding group of genetic disorders which encompass a spectrum of glycosylation defects of protein and lipids, including N- & O-linked defects and among the latter are the muscular ...
Bliss, E, Carreno, G, Clayton, PT, Grunewald, S, Heywood, WE, Mills, K, Mills, P, Muntoni, F, Sebire, NJ, Torelli, S, Worthington, VC, Yuzugulen, J   +11 more
core   +2 more sources

Mosaicism of the UDP-Galactose transporter SLC35A2 in a female causing a congenital disorder of glycosylation: a case report

BMC Medical Genetics, 2018
Background Congenital disorders of glycosylation are rare conditions caused by genetic defects in glycan synthesis, processing or transport. Most congenital disorders of glycosylation involve defects in the formation or transfer of the lipid-linked ...
Kristen Westenfield, Kyriakie Sarafoglou, Laura C. Speltz, Elizabeth I. Pierpont, Joan Steyermark, David Nascene, Matthew Bower, Mary Ella Pierpont   +7 more
doaj   +1 more source

Liver manifestations in a cohort of 39 patients with congenital disorders of glycosylation: pin-pointing the characteristics of liver injury and proposing recommendations for follow-up

Orphanet Journal of Rare Diseases, 2021
Background The congenital disorders of glycosylation (CDG) are a heterogeneous group of rare metabolic diseases with multi-system involvement. The liver phenotype of CDG varies not only according to the specific disorder, but also from patient to patient.
Rodrigo Tzovenos Starosta, Suzanne Boyer, Shawn Tahata, Kimiyo Raymond, Hee Eun Lee, Lynne A. Wolfe, Christina Lam, Andrew C. Edmondson, Ida Vanessa Doederlein Schwartz, Eva Morava   +9 more
doaj   +1 more source

PMM2-CDG T237M Mutation in a Patient with Cerebral Palsy-Like Phenotypes Reported from South India

Global Medical Genetics, 2023
Congenital disorder of glycosylation (CDG) is an autosomal recessively inherited disorder. Hypotonia, stroke-like episodes, and peripheral neuropathy are also associated with the condition that typically develops during infancy.
N. Sreedevi, N. Swapna, Santosh Maruthy, H.S. Meghavathi, Charles Sylvester   +4 more
doaj   +1 more source

Congenital disorders of glycosylation (CDG): state of the art in 2022

Orphanet Journal of Rare Diseases, 2023
AbstractCongenital disorders of glycosylation (CDG) are a complex and heterogeneous family of rare metabolic diseases. With a clinical history that dates back over 40 years, it was the recent multi-omics advances that mainly contributed to the fast-paced and encouraging developments in the field.
Francisco, Rita, Brasil, Sandra, Poejo, Joana, Jaeken, Jaak, Pascoal, Carlota, Videira, Paula A., Ferreira, Vanessa dos Reis   +6 more
openaire   +4 more sources

Bridging the Gap between Glycosylation and Vesicle Traffic [PDF]

, 2016
Glycosylation is recognized as a vitally important posttranslational modification. The structure of glycans that decorate proteins and lipids is largely dictated by biosynthetic reactions occurring in the Golgi apparatus.
Abdul Rahman, Axelsson, Baas, Baker, Banfield, Bentley, Carr, Cheung, Cottam, Cottam, Dejgaard, Demircioglu, Drin, Eckert, Faid, Foulquier, Fridmann-Sirkis, Fukuda, Gawlitzek, Gilchrist, Gillingham, Grasa, Ha, Hassinen, Hennet, Hong, Hutagalung, Huybrechts, Ioffe, Jarvela, Joshi, Kelly, Kingsley, Kodera, Koreishi, Kornak, Kornfeld, Kosodo, Kranz, Kudlyk, Laufman, Laufman, Laufman, Lees, Lobingier, Lübbehusen, Maeda, Malsam, McDonald, McNew, Miller, Miller, Miserey-Lenkei, Misura, Nairn, Oka, Ong, Orci, Paesold-Burda, Papanikou, Park, Patterson, Peanne, Peng, Petrosyan, Petrosyan, Pfeffer, Pokrovskaya, Puthenveedu, Rabouille, Reynders, Rivinoja, Rymen, Rymen, Sato, Schmitz, Schnorrer, Setty, Sharpe, Shestakova, Shi, Sinka, Smits, Sohda, Sohda, Stanley, Starr, Steet, Struwe, Suvorova, Togneri, Tu, Uemura, Ungar, van Galen, Willett, Willett, Witkos, Wong, Wu, Xiang, Xu, Yamaguchi, Yamane, Ye, Yu   +105 more
core   +5 more sources